메뉴 건너뛰기




Volumn , Issue , 2011, Pages

Hsp27-actin interaction

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84855269873     PISSN: 20902247     EISSN: 20902255     Source Type: Journal    
DOI: 10.1155/2011/901572     Document Type: Article
Times cited : (19)

References (47)
  • 1
    • 0035718677 scopus 로고    scopus 로고
    • Structure and function of the small heat shock protein/crystallin family of molecular chaperones
    • DOI 10.1016/S0065-3233(01)59004-X
    • Van Montfort R., Slingsby C., Vierling E., Structure and function of the small heat shock protein/ -crystallin family of molecular chaperones Advances in Protein Chemistry 2001 59 105 156 (Pubitemid 34169303)
    • (2001) Advances in Protein Chemistry , vol.59 , pp. 105-156
    • Van Montfort, R.1    Slingsby, C.2    Vierling, E.3
  • 2
    • 0036556697 scopus 로고    scopus 로고
    • Actin cytoskeleton and small heat shock proteins: How do they interact?
    • DOI 10.1379/1466-1268(2002)007<0167:ACASHS>2.0.CO;2
    • Mounier N., Arrigo A. P., Actin cytoskeleton and small heat shock proteins: how do they interact? Cell Stress and Chaperones 2002 7 2 167 176 (Pubitemid 36133467)
    • (2002) Cell Stress and Chaperones , vol.7 , Issue.2 , pp. 167-176
    • Mounier, N.1    Arrigo, A.-P.2
  • 3
    • 0036558366 scopus 로고    scopus 로고
    • Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins
    • DOI 10.1023/A:1015549725819
    • Gusev N. B., Bogatcheva N. V., Marston S. B., Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins Biochemistry (Moscow) 2002 67 5 511 519 (Pubitemid 34719953)
    • (2002) Biochemistry (Moscow) , vol.67 , Issue.5 , pp. 511-519
    • Gusev, N.B.1    Bogatcheva, N.V.2    Marston, S.B.3
  • 4
  • 5
    • 0031849099 scopus 로고    scopus 로고
    • Small heat-shock protein family: Function in health and disease
    • DOI 10.1111/j.1749-6632.1998.tb08973.x
    • Welsh M. J., Gaestel M., Small heat-shock protein family: function in health and disease Annals of the New York Academy of Sciences 1998 851 28 35 (Pubitemid 28370360)
    • (1998) Annals of the New York Academy of Sciences , vol.851 , pp. 28-35
    • Welsh, M.J.1    Gaestel, M.2
  • 6
    • 0033968166 scopus 로고    scopus 로고
    • Small heat-shock proteins and their potential role in human disease
    • DOI 10.1016/S0959-440X(99)00048-2
    • Clark J. I., Muchowski P. J., Small heat-shock proteins and their potential role in human disease Current Opinion in Structural Biology 2000 10 1 52 59 (Pubitemid 30099327)
    • (2000) Current Opinion in Structural Biology , vol.10 , Issue.1 , pp. 52-59
    • Clark, J.I.1    Muchowski, P.J.2
  • 7
    • 20444478694 scopus 로고    scopus 로고
    • The small heat shock proteins and their role in human disease
    • DOI 10.1111/j.1742-4658.2005.04708.x
    • Sun Y., MacRae T. H., The small heat shock proteins and their role in human disease FEBS Journal 2005 272 11 2613 2627 (Pubitemid 40825410)
    • (2005) FEBS Journal , vol.272 , Issue.11 , pp. 2613-2627
    • Sun, Y.1    MacRae, T.H.2
  • 8
    • 27144448839 scopus 로고    scopus 로고
    • Some like it hot: The structure and function of small heat-shock proteins
    • DOI 10.1038/nsmb993, PII N993
    • Haslbeck M., Franzmann T., Weinfurtner D., Buchner J., Some like it hot: the structure and function of small heat-shock proteins Nature Structural and Molecular Biology 2005 12 10 842 846 (Pubitemid 41486706)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.10 , pp. 842-846
    • Haslbeck, M.1    Franzmann, T.2    Weinfurtner, D.3    Buchner, J.4
  • 10
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • DOI 10.1016/S0092-8674(03)00120-X
    • Pollard T. D., Borisy G. G., Cellular motility driven by assembly and disassembly of actin filaments Cell 2003 112 4 453 465 (Pubitemid 36263079)
    • (2003) Cell , vol.112 , Issue.4 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 11
    • 0027417852 scopus 로고
    • Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock. HSP27 stabilization of the microfilament organization
    • Lavoie J. N., Gingras-Breton G., Tanguay R. M., Landry J., Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock. HSP27 stabilization of the microfilament organization Journal of Biological Chemistry 1993 268 5 3420 3429 (Pubitemid 23070978)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.5 , pp. 3420-3429
    • Lavoie, J.N.1    Gingras-Breton, G.2    Tanguay, R.M.3    Landry, J.4
  • 12
    • 0027482463 scopus 로고
    • Modulation of actin-microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27
    • Lavoie J. N., Hickey E., Weber L. A., Landry J., Modulation of actin-microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27 Journal of Biological Chemistry 1993 268 32 24210 24214 (Pubitemid 23335406)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.32 , pp. 24210-24214
    • Lavoie, J.N.1    Hickey, E.2    Weber, L.A.3    Landry, J.4
  • 13
    • 0027937934 scopus 로고
    • Phosphorylated HSP27 associates with the activation-dependent cytoskeleton in human platelets
    • Zhu Y., O'Neill S., Saklatvala J., Tassi L., Mendelsohn M. E., Phosphorylated HSP27 associates with the activation-dependent cytoskeleton in human platelets Blood 1994 84 11 3715 3723 (Pubitemid 24362468)
    • (1994) Blood , vol.84 , Issue.11 , pp. 3715-3723
    • Zhu, Y.1    O'Neill, S.2    Saklatvala, J.3    Tassi, L.4    Mendelsohn, M.E.5
  • 14
    • 0028924759 scopus 로고
    • Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27
    • Lavoie J. N., Lambert H., Hickey E., Weber L. A., Landry J., Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27 Molecular and Cellular Biology 1995 15 1 505 516 (Pubitemid 24379949)
    • (1995) Molecular and Cellular Biology , vol.15 , Issue.1 , pp. 505-516
    • Lavoie, J.N.1    Lambert, H.2    Hickey, E.3    Weber, L.A.4    Landry, J.5
  • 15
    • 0030069517 scopus 로고    scopus 로고
    • HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress
    • Huot J., Houle F., Spitz D. R., Landry J., HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress Cancer Research 1996 56 2 273 279 (Pubitemid 26026354)
    • (1996) Cancer Research , vol.56 , Issue.2 , pp. 273-279
    • Huot, J.1    Houle, F.2    Spitz, D.R.3    Landry, J.4
  • 16
    • 0031057892 scopus 로고    scopus 로고
    • Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells
    • Huot J., Houle F., Marceau F., Landry J., Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells Circulation Research 1997 80 3 383 392 (Pubitemid 27093353)
    • (1997) Circulation Research , vol.80 , Issue.3 , pp. 383-392
    • Huot, J.1    Houle, F.2    Marceau, F.3    Landry, J.4
  • 17
    • 0031056783 scopus 로고    scopus 로고
    • Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27
    • Guay J., Lambert H., Gingras-Breton G., Lavoie J. N., Huot J., Landry J., Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27 Journal of Cell Science 1997 110 3 357 368 (Pubitemid 27095655)
    • (1997) Journal of Cell Science , vol.110 , Issue.3 , pp. 357-368
    • Guay, J.1    Lambert, H.2    Gingras-Breton, G.3    Lavoie, J.N.4    Huot, J.5    Landry, J.6
  • 18
    • 0030734010 scopus 로고    scopus 로고
    • P38 MAP kinase activation by vascular endothelial growth factor mediates actin reorganization and cell migration in human endothelial cells
    • Rousseau S., Houle F., Landry J., Huot J., P38 MAP kinase activation by vascular endothelial growth factor mediates actin reorganization and cell migration in human endothelial cells Oncogene 1997 15 18 2169 2177 (Pubitemid 27493906)
    • (1997) Oncogene , vol.15 , Issue.18 , pp. 2169-2177
    • Rousseau, S.1    Houle, F.2    Landry, J.3    Huot, J.4
  • 19
    • 0031772351 scopus 로고    scopus 로고
    • In vivo evaluation of hsp27 as an inhibitor of actin polymerization: Hsp27 limits actin stress fiber and focal adhesion formation after heat shock
    • DOI 10.1002/(SICI)1097-4652(199812)177:4<575::AID-JCP8>3.0.CO;2-1
    • Schneider G. B., Hamano H., Cooper L. F., In vivo evaluation of hsp27 as an inhibitor of actin polymerization: Hsp27 limits actin stress fiber and focal adhesion formation after heat shock Journal of Cellular Physiology 1998 177 4 575 584 (Pubitemid 28541582)
    • (1998) Journal of Cellular Physiology , vol.177 , Issue.4 , pp. 575-584
    • Schneider, G.B.1    Hamano, H.2    Cooper, L.F.3
  • 21
  • 23
    • 3042730951 scopus 로고    scopus 로고
    • Control of actin dynamics by p38 MAP kinase - Hsp27 distribution in the lamellipodium of smooth muscle cells
    • DOI 10.1242/jcs.01110
    • Pichon S., Bryckaert M., Berrou E., Control of actin dynamics by p38 MAP kinaseHsp27 distribution in the lamellipodium of smooth muscle cells Journal of Cell Science 2004 117 12 2569 2577 (Pubitemid 38877852)
    • (2004) Journal of Cell Science , vol.117 , Issue.12 , pp. 2569-2577
    • Sebastien, P.1    Bryckaert, M.2    Berrou, E.3
  • 24
    • 34247643279 scopus 로고    scopus 로고
    • Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation
    • DOI 10.1038/sj.emboj.7601687, PII 7601687
    • During R. L., Gibson B. G., Li W., Bishai E. A., Sidhu G. S., Landry J., Southwick F. S., Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation EMBO Journal 2007 26 9 2240 2250 (Pubitemid 46685867)
    • (2007) EMBO Journal , vol.26 , Issue.9 , pp. 2240-2250
    • During, R.L.1    Gibson, B.G.2    Li, W.3    Bishai, E.A.4    Sidhu, G.S.5    Landry, J.6    Southwick, F.S.7
  • 25
    • 77950866609 scopus 로고    scopus 로고
    • The role of Hsp27 and actin in the regulation of movement in human cancer cells responding to heat shock
    • Doshi B. M., Hightower L. E., Lee J., The role of Hsp27 and actin in the regulation of movement in human cancer cells responding to heat shock Cell Stress and Chaperones 2009 14 5 445 457
    • (2009) Cell Stress and Chaperones , vol.14 , Issue.5 , pp. 445-457
    • Doshi, B.M.1    Hightower, L.E.2    Lee, J.3
  • 26
    • 0024212723 scopus 로고
    • Characterization of an inhibitor of actin polymerization in vinculin-rich fraction of turkey gizzard smooth muscle
    • DOI 10.1111/j.1432-1033.1988.tb14481.x
    • Miron T., Wilchek M., Geiger B., Characterization of an inhibitor of actin polymerization in vinculin-rich fraction of turkey gizzard smooth muscle European Journal of Biochemistry 1988 178 2 543 553 (Pubitemid 19021857)
    • (1988) European Journal of Biochemistry , vol.178 , Issue.2 , pp. 543-553
    • Miron, T.1    Wilchek, M.2    Geiger, B.3
  • 27
    • 9644260484 scopus 로고    scopus 로고
    • Self-association of a small heat shock protein
    • DOI 10.1016/j.jmb.2004.10.056, PII S0022283604013610
    • Lelj-Garolla B., Mauk A. G., Self-association of a small heat shock protein Journal of Molecular Biology 2005 345 3 631 642 (Pubitemid 39575929)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.3 , pp. 631-642
    • Lelj-Garolla, B.1    Mauk, A.G.2
  • 29
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee J. D., Purification of muscle actin Methods in Enzymology 1982 85 164 181
    • (1982) Methods in Enzymology , vol.85 , pp. 164-181
    • Pardee, J.D.1
  • 30
    • 0016294918 scopus 로고
    • The measurement of actin concentration in solution: A comparison of methods
    • Houk T. W., and Ue K., The measurement of actin concentration in solution: a comparison of methods Analytical Biochemistry 1974 62 1 66 74
    • (1974) Analytical Biochemistry , vol.62 , Issue.1 , pp. 66-74
    • Houk, T.W.1    Ue, K.2
  • 31
    • 0033972325 scopus 로고    scopus 로고
    • Subunit exchange of small heat shock proteins. Analysis of oligomer formation of A-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations
    • DOI 10.1074/jbc.275.2.1035
    • Bova M. P., Mchaourab H. S., Han Y., Fung B. K. K., Subunit exchange of small heat shock proteins. Analysis of oligomer formation of A-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations Journal of Biological Chemistry 2000 275 2 1035 1042 (Pubitemid 30051151)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.2 , pp. 1035-1042
    • Bova, M.P.1    Mchaourab, H.S.2    Han, Y.3    Fung, B.K.-K.4
  • 32
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • DOI 10.1016/0003-2697(85)90442-7
    • Smith P. K., Krohn R. I., Hermanson G. T., Measurement of protein using bicinchoninic acid Analytical Biochemistry 1985 150 1 76 85 (Pubitemid 16258399)
    • (1985) Analytical Biochemistry , vol.150 , Issue.1 , pp. 76-85
    • Smith, P.K.1    Krohn, R.I.2    Hermanson, G.T.3
  • 33
    • 0021112116 scopus 로고
    • Synthesis, spectral properties, and use of 6-acryloyl-2- dimethylaminonaphthalene (Acrylodan). A thiol-selective, polarity-sensitive fluorescent probe
    • Prendergast F. G., Meyer M., Carlson G. L., Iida S., Potter J. D., Synthesis, spectral properties, and use of 6-acryloyl-2-dimethylaminonaphthalene (Acrylodan). A thiol-selective, polarity-sensitive fluorescent probe Journal of Biological Chemistry 1983 258 12 7541 7544
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.12 , pp. 7541-7544
    • Prendergast, F.G.1    Meyer, M.2    Carlson, G.L.3    Iida, S.4    Potter, J.D.5
  • 34
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin
    • Kouyama T., Mihashi K., Fluorimetry study of N-(1-pyrenyl)iodoacetamide- labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin European Journal of Biochemistry 1981 114 1 33 38 (Pubitemid 11101489)
    • (1981) European Journal of Biochemistry , vol.114 , Issue.1 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 35
    • 0021251356 scopus 로고
    • Troponin-Tropomyosin interactions. Fluorescence studies of the binding of troponin, troponin T, and chymotryptic troponin T fragments to specifically labeled tropomyosin
    • Morris E. P., Lehrer S. S., Troponin-tropomyosin interactions. Fluorescence studies of the binding of troponin, troponin T, and chymotryptic troponin T fragments to specifically labeled tropomyosin Biochemistry 1984 23 10 2214 2220 (Pubitemid 14110725)
    • (1984) Biochemistry , vol.23 , Issue.10 , pp. 2214-2220
    • Morris, E.P.1    Lehrer, S.S.2
  • 36
    • 0034680855 scopus 로고    scopus 로고
    • An extended conformation of calmodulin induces interactions between the structural domains of adenylyl cyclase from Bacillus anthracis to promote catalysis
    • Drum C. L., Yan S. Z., Sarac R., Mabuchi Y., Beckingham K., Bohm A., Grabarek Z., Tang W. J., An extended conformation of calmodulin induces interactions between the structural domains of adenylyl cyclase from Bacillus anthracis to promote catalysis Journal of Biological Chemistry 2000 275 46 36334 36340
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.46 , pp. 36334-36340
    • Drum, C.L.1    Yan, S.Z.2    Sarac, R.3    Mabuchi, Y.4    Beckingham, K.5    Bohm, A.6    Grabarek, Z.7    Tang, W.J.8
  • 37
    • 0028672523 scopus 로고
    • Boundary analysis in sedimentation velocity experiments
    • Stafford W. F. III, Boundary analysis in sedimentation velocity experiments Methods in Enzymology 1994 240 478 501
    • (1994) Methods in Enzymology , vol.240 , pp. 478-501
    • Stafford III, W.F.1
  • 38
    • 0033040618 scopus 로고    scopus 로고
    • Effect of capping protein, CapZ, on the length of actin filaments and mechanical properties of actin filament networks
    • DOI 10.1002/(SICI)1097-0169(1999)42:1<73::AID-CM7>3.0.CO;2-Z
    • Xu J., Casella J. F., Pollard T. D., Effect of capping protein, CapZ, on the length of actin filaments and mechanical properties of actin filament networks Cell Motility and the Cytoskeleton 1999 42 1 73 81 (Pubitemid 29144325)
    • (1999) Cell Motility and the Cytoskeleton , vol.42 , Issue.1 , pp. 73-81
    • Xu, J.1    Casella, J.F.2    Pollard, T.D.3
  • 39
    • 0029202621 scopus 로고
    • Pyrene excimer fluorescence as a probe of protein conformational change
    • Lehrer S. S., Pyrene excimer fluorescence as a probe of protein conformational change Sub-cellular biochemistry 1995 24 115 132
    • (1995) Sub-cellular Biochemistry , vol.24 , pp. 115-132
    • Lehrer, S.S.1
  • 40
    • 0030919291 scopus 로고    scopus 로고
    • Intramolecular pyrene excimer fluorescence: A probe of proximity and protein conformational change
    • DOI 10.1016/S0076-6879(97)78015-7
    • Lehrer S. S., Intramolecular pyrene excimer fluorescence: a probe of proximity and protein conformational change Methods in Enzymology 1997 278 286 295 (Pubitemid 27229924)
    • (1997) Methods in Enzymology , vol.278 , pp. 286-295
    • Lehrer, S.S.1
  • 41
    • 0033525723 scopus 로고    scopus 로고
    • Site-directed spin labeling study of subunit interactions in the - crystallin domain of small heat-shock proteins. Comparison of the oligomer symmetry in A-crystallin, HSP 27, and HSP 16.3
    • DOI 10.1074/jbc.274.10.6305
    • Berengian A. R., Parfenova M., McHaourab H. S., Site-directed spin labeling study of subunit interactions in the -crystallin domain of small heat-shock proteins. Comparison of the oligomer symmetry in A-crystallin, HSP 27, and HSP 16.3 Journal of Biological Chemistry 1999 274 10 6305 6314 (Pubitemid 29111042)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.10 , pp. 6305-6314
    • Berengian, A.R.1    Parfenova, M.2    McHaourab, H.S.3
  • 42
    • 0030732692 scopus 로고    scopus 로고
    • Site-directed spin-labeling study of the structure and subunit interactions along a conserved sequence in the crystallin domain of heat- shock protein 27. Evidence of a conserved subunit interface
    • DOI 10.1021/bi971700s
    • Mchaourab H. S., Berengian A. R., Koteiche H. A., Site-directed spin-labeling study of the structure and subunit interactions along a conserved sequence in the -crystallin domain of heat- shock protein 27. Evidence of a conserved subunit interface Biochemistry 1997 36 48 14627 14634 (Pubitemid 27524382)
    • (1997) Biochemistry , vol.36 , Issue.48 , pp. 14627-14634
    • Mchaourab, H.S.1    Berengian, A.R.2    Koteiche, H.A.3
  • 43
    • 0032077161 scopus 로고    scopus 로고
    • The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25
    • DOI 10.1016/S0141-8130(98)00014-2, PII S0141813098000142
    • Zavialov A., Benndorf R., Ehrnsperger M., Zav'Yalov V., Dudich I., Buchner J., Gaestel M., The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25 International Journal of Biological Macromolecules 1998 22 3-4 163 173 (Pubitemid 28276730)
    • (1998) International Journal of Biological Macromolecules , vol.22 , Issue.3-4 , pp. 163-173
    • Zavialov, A.1    Benndorf, R.2    Ehrnsperger, M.3    Zav'Yalov, V.4    Dudich, I.5    Buchner, J.6    Gaestel, M.7
  • 45
    • 0028071812 scopus 로고
    • Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity
    • Benndorf R., Hayess K., Ryazantsev S., Wieske M., Behlke J., Lutsch G., Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity Journal of Biological Chemistry 1994 269 32 20780 20784 (Pubitemid 24260495)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.32 , pp. 20780-20784
    • Benndorf, R.1    Hayess, K.2    Ryazantsev, S.3    Wieske, M.4    Behlke, J.5    Lutsch, G.6
  • 46
    • 77954412855 scopus 로고    scopus 로고
    • Vinculin is a dually regulated actin filament barbed end-capping and side-binding protein
    • Le Clainche C., Dwivedi S. P., Didry D., Carlier M. F., Vinculin is a dually regulated actin filament barbed end-capping and side-binding protein Journal of Biological Chemistry 2010 285 30 23420 23432
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.30 , pp. 23420-23432
    • Le Clainche, C.1    Dwivedi, S.P.2    Didry, D.3    Carlier, M.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.